Summary: Mannitol dehydrogenase C-terminal domain
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Mannitol dehydrogenase C-terminal domain Provide feedback
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This tab holds annotation information from the InterPro database.
InterPro entry IPR013118
Long-chain mannitol dehydrogenases are a group of secondary alcohol dehydrogenases that differ from other alcohol or polyol dehydrogenases in that they do not utilise Zn(2+) or other metal cofactors and do not contain a conserved catalytic tyrosine residue. The proteins in this family that have been studied are monomeric enzymes of ~54 kDa and include:
- Mannitol-1-phosphate 5-dehydrogenase (EC) [PUBMED:11160802]
- Mannitol 2-dehydrogenase (EC) [PUBMED:8254318]
- D-arabinitol 4-dehydrogenase (EC) [PUBMED:9639934]
- Altronate oxidoreductase (EC)
- D-mannonate oxidoreductase (EC)
This entry represents the C-terminal substrate-binding domain of long-chain mannitol dehydrogenases. This domain is primarily alpha-helical in nature, being composed of eleven helices and a small beta hairpin [PUBMED:12196534]. Most of the residues implicated in substrate binding are located within this region, and a conserved lysine residue is thought to act as a proton acceptor during catalysis.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||coenzyme binding (GO:0050662)|
|oxidoreductase activity (GO:0016491)|
|Biological process||oxidation-reduction process (GO:0055114)|
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Curation and family details
|Number in seed:||13|
|Number in full:||26626|
|Average length of the domain:||235.20 aa|
|Average identity of full alignment:||34 %|
|Average coverage of the sequence by the domain:||52.75 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||9|
|Download:||download the raw HMM for this family|
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There are 2 interactions for this family. More...
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Mannitol_dh_C domain has been found. There are 5 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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